| phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
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| phosphorylase a | <enzyme> The phosphorylated and more active form of phosphorylase that functions as a regulatory enzyme during glycogen breakdown. The phosphate groups are hydrolytically removed by phosphorylase phosphatase to form phosphorylase b and orthophosphate. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase b | <enzyme> The relatively inactive form of phosphorylase that is reactivated to form phosphorylase a by phosphorylase kinase, which catalyses the enzymatic phosphorylation of the serine residues at the expense of ATP. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase kinase | <enzyme> The enzyme that regulates the activity of phosphorylase and glycogen synthetase by addition of phosphate groups. A large and complex enzyme, itself regulated by phosphorylation. Integrates the hormonal and calcium signals in muscle. (18 Nov 1997) |
| phosphorylase kinase phosphatase | <enzyme> Aspect of phosphoprotein phosphatase EC 3.1.3.16 Registry number: EC 3.1.3.- (26 Jun 1999) |
| phosphorylase phosphatase | <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. Chemical name: (Phosphorylase a) phosphohydrolase Registry number: EC 3.1.3.17 (12 Dec 1998) |
| phosphorylase-rupturing enzyme | <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. Chemical name: (Phosphorylase a) phosphohydrolase Registry number: EC 3.1.3.17 (12 Dec 1998) |
| phosphorylases | 1. General term for enzymes transferring an inorganic phosphate group to some organic acceptor, hence belonging to the transferases. 2. Specifically, enzymes that release a single glucosyl residue from a polyglucose as d-glucose 1-phosphate, the phosphate coming from inorganic orthophosphate; e.g., phosphophorylase, sucrose phosphorylases, cellobiose phosphorylases. (05 Mar 2000) |
| alpha,alpha-trehalose phosphorylase | <enzyme> Chemical name: alpha-d-glucopyranosyl-alpha-d-glucopyranose orthophosphate glucosyltransferase Registry number: EC 2.4.1.64 Synonym: trehalose phosphorylase (26 Jun 1999) |
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| alpha-glucan phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| maltodextrin phosphorylase | <enzyme> From E coli Registry number: EC 2.4.1.- Synonym: e350a (26 Jun 1999) |
| GDPmannose phosphorylase | <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate. Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases Registry number: EC 2.7.7.13 Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein (26 Jun 1999) |
| cellodextrin phosphorylase | <enzyme> Reverse reaction is used to synthesise cellodextrins Registry number: EC 2.4.1.49 (26 Jun 1999) |
| glycogen phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| muscle phosphorylase deficiency | Type V glycogen storage disease, affecting muscle, caused by deficiency of muscle phosphorylase. (05 Mar 2000) |
| polynucleotide phosphorylase | <enzyme> An enzyme of the transferase class that catalyses the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, idp, GDP, udp, and cdp can act as donors in the latter case. Chemical name: Polyribonucleotide:orthophosphate nucleotidyltransferase Registry number: EC 2.7.7.8 (12 Dec 1998) |
| xanthosine phosphorylase | <enzyme> From E coli k-12; mw 18kda; inactivated by p-chloromercuriphenylsulfonic acid Registry number: EC 2.4.2.- Synonym: inosine-guanosine phosphorylase (26 Jun 1999) |
| purine-nucleoside phosphorylase | <enzyme> An enzyme that catalyses the reaction between a purine nucleoside and orthophosphate to form a free purine plus ribose-5-phosphate. Chemical name: Purine-nucleoside:orthophosphate ribosyltransferase Registry number: EC 2.4.2.1 (12 Dec 1998) |
| pyrimidine-nucleoside phosphorylase | <enzyme> Consider uridine phosphorylase and thymidine phosphorylase Registry number: EC 2.4.2.2 Synonym: pyrimidine nucleoside phosphorylase (26 Jun 1999) |
| nucleoside phosphorylase | <enzyme> From klebsiella sp.; acts on both purine and pyrimidine nucleosides and catalyses the production of araa from uridine arabinoside (arau) and adenine Registry number: EC 2.4.2.- (26 Jun 1999) |
| diadenosine 5,5'''-P(1),P(4)-tetraphosphate alpha,beta-phosphorylase | <enzyme> Ap4a + inorganic po4 forms ATP + ADP Registry number: EC 2.7.7.53 Synonym: ap4a phosphorylase, ATP adenylyltransferase (26 Jun 1999) |
| orotidylic acid phosphorylase | <enzyme> The enzyme catalyzing the formation of orotidine-5'-phosphoric acid (orotidylic acid) from orotic acid and 5-phosphoribosyl-1-pyrophosphate in the course of pyrimidine nucleotide biosynthesis. Chemical name: Orotidine-5'-phosphate:pyrophosphate phospho-alpha-D-ribosyltransferase Registry number: EC 2.4.2.10 (12 Dec 1998) |
| thymidine phosphorylase | <enzyme> The enzyme catalyzing the transfer of 2-deoxy-d-ribose from thymidine to orthophosphate, thereby liberating thymidine. Chemical name: Thymidine:orthophosphate deoxy-D-ribosyltransferase Registry number: EC 2.4.2.4 (12 Dec 1998) |